3rlq: Difference between revisions
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New page: '''Unreleased structure''' The entry 3rlq is ON HOLD Authors: Kung, P-P., Sinnema, P-J., Richardson, P., Hickey, M.J., Gajiwala, K.S., Wang, F., Huang, B., McClellan, G., Wang, J., Maeg... |
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==Co-crystal structure of the HSP90 ATP binding domain in complex with 4-(2,4-dichloro-5-methoxyphenyl)-2-methyl-7H-pyrrolo[2,3-d]pyrimidine-5- carbonitrile== | |||
<StructureSection load='3rlq' size='340' side='right'caption='[[3rlq]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3rlq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RLQ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3RQ:4-(2,4-DICHLORO-5-METHOXYPHENYL)-2-METHYL-7H-PYRROLO[2,3-D]PYRIMIDINE-5-CARBONITRILE'>3RQ</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rlq OCA], [https://pdbe.org/3rlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rlq RCSB], [https://www.ebi.ac.uk/pdbsum/3rlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rlq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref> | |||
==See Also== | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Bergqvist S]] | |||
[[Category: Gajiwala KS]] | |||
[[Category: Hickey MJ]] | |||
[[Category: Huang B]] | |||
[[Category: Kania R]] | |||
[[Category: Kung P-P]] | |||
[[Category: Maegley K]] | |||
[[Category: McClellan G]] | |||
[[Category: Mehta PP]] | |||
[[Category: Richardson P]] | |||
[[Category: Sinnema P-J]] | |||
[[Category: Wang F]] | |||
[[Category: Wang J]] | |||
Latest revision as of 09:43, 1 March 2024
Co-crystal structure of the HSP90 ATP binding domain in complex with 4-(2,4-dichloro-5-methoxyphenyl)-2-methyl-7H-pyrrolo[2,3-d]pyrimidine-5- carbonitrile
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